Prehm S, Nickel V, Prehm P
Institut für Physiologische Chemie und Pathobiochemie, Münster, Germany.
Protein Expr Purif. 1996 Jun;7(4):343-6. doi: 10.1006/prep.1996.0051.
A new method was developed to purify the streptococcal hyaluronate synthase in active form to electrophoretic homogeneity. The method is based on the extraction of protoplast membranes with digitonin and a phase separation into an aqueous and a detergent phase induced by addition of polyethylene glycol 6000 at 0 degree C. Proteins bound to hyaluronate were enriched in the aqueous phase, whereas other membrane proteins resided in the detergent phase. Final purification of the hyaluronate synthase was achieved by ion exchange chromatography.
已开发出一种新方法，可将活性形式的链球菌透明质酸合酶纯化至电泳纯。该方法基于用洋地黄皂苷提取原生质体膜，并在0℃下通过添加聚乙二醇6000诱导相分离成水相和去污剂相。与透明质酸结合的蛋白质富集于水相中，而其他膜蛋白则存在于去污剂相中。透明质酸合酶的最终纯化通过离子交换色谱法实现。
